English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Opposing effects of folding and assembly chaperones on evolvability of Rubisco

Durao, P., Aigner, H., Nagy, P., Mueller-Cajar, O., Hartl, F. U., & Hayer-Hartl, M. (2015). Opposing effects of folding and assembly chaperones on evolvability of Rubisco. NATURE CHEMICAL BIOLOGY, 11(2), 148-155. doi:10.1038/NCHEMBIO.1715.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-7335-E Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0025-7336-C
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Durao, Paulo1, Author              
Aigner, Harald1, Author              
Nagy, Peter1, Author              
Mueller-Cajar, Oliver1, Author              
Hartl, F. Ulrich1, Author              
Hayer-Hartl, Manajit2, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

Content

show
hide
Free keywords: RIBULOSE-BISPHOSPHATE CARBOXYLASE; ESCHERICHIA-COLI; RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE; HEXADECAMERIC RUBISCO; DIRECTED EVOLUTION; PROTEIN EVOLUTION; SEQUENCE SPACE; ENZYME; OXYGENASE; SELECTION
 Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) catalyzes the fixation of CO2 in photosynthesis. Despite its pivotal role, Rubisco is an inefficient enzyme and thus is a key target for directed evolution. Rubisco biogenesis depends on auxiliary factors, including the GroEL/ES-type chaperonin for folding and the chaperone RbcX for assembly. Here we performed directed evolution of cyanobacterial form I Rubisco using a Rubisco-dependent Escherichia coli strain. Overexpression of GroEL/ES enhanced Rubisco solubility and tended to expand the range of permissible mutations. In contrast, the specific assembly chaperone RbcX had a negative effect on evolvability by preventing a subset of mutants from forming holoenzyme. Mutation F140I in the large Rubisco subunit, isolated in the absence of RbcX, increased carboxylation efficiency approximately threefold without reducing CO2 specificity. The F140I mutant resulted in a similar to 55% improved photosynthesis rate in Synechocystis PCC6803. The requirement of specific biogenesis factors downstream of chaperonin may have retarded the natural evolution of Rubisco.

Details

show
hide
Language(s): eng - English
 Dates: 2015-02
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: ISI: 000348358800013
DOI: 10.1038/NCHEMBIO.1715
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: NATURE CHEMICAL BIOLOGY
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 11 (2) Sequence Number: - Start / End Page: 148 - 155 Identifier: ISSN: 1552-4450